|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
34-560 |
0e+00 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 543.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 34 SGGRGRAWLQPTGR---ETGVQVYNSLTGRKEPLIVAHAEAASWYSCGPTVYDHAHLGHACSYVRFDIIRRILTKVFGCN 110
Cdd:PTZ00399 20 SKSRLPEWKKPSKEgkyLTGLKVNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRILEDYFGYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 111 IVMVMGITDVDDKIIKRANEMNISPAS-LASLYEEDFKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGHAYStAK 189
Cdd:PTZ00399 100 VFYVMNITDIDDKIIKRAREEKLSIFLeLARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYE-SN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 190 GNVYFDLKS-RGDK--YGKLVgvvPGPV--------GEPA----DSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHI 254
Cdd:PTZ00399 179 GSVYFDVEAfRKAGhvYPKLE---PESVadedriaeGEGAlgkvSGEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 255 ECSAIASMVFGSQLDIHSGGIDLAFPHHENEIAQCEVFHQCEQWGNYFLHSGHLHVKGkeEKMSKSLKNYITIKDFLKTF 334
Cdd:PTZ00399 256 ECSAMASNILGDPIDIHSGGIDLKFPHHDNELAQSEAYFDKHQWVNYFLHSGHLHIKG--LKMSKSLKNFITIRQALSKY 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 335 SPDVFRFFCLRSSYRSAIDYSDSAMLHAQQQLLALGSFLEDARAYMKgQLACGSVR-----EVMLWERLASTRSAVKEAL 409
Cdd:PTZ00399 334 TARQIRLLFLLHKWDKPMNYSDESMDEAIEKDKVFFNFFANVKIKLR-ESELTSPQkwtqhDFELNELFEETKSAVHAAL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 410 ADDFDTPRVVDAILGLAHHGNGQLRAASKepgvPRSPAVFgAIISYFEQFFETVGISLGNQQCVSGD--GSEATLRGVVE 487
Cdd:PTZ00399 413 LDNFDTPEALQALQKLISATNTYLNSGEQ----PSAPLLR-SVAQYVTKILSIFGLVEGSDGLGSQGqnSTSENFKPLLE 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622884557 488 ELVRFRQKVRQFalAKAEATGEARRQQLlerQPLLEACDTLR-QDLTAHGISIKDRNSTTSTWELLD----QRTKDQK 560
Cdd:PTZ00399 488 ALLRFRDEVRDA--AKAEMKLISLDKKK---KQLLQLCDKLRdEWLPNLGIRIEDKPDGPSVWKLDDkeelQREKEEK 560
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
52-551 |
5.00e-174 |
|
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439985 [Multi-domain] Cd Length: 465 Bit Score: 500.01 E-value: 5.00e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 52 QVYNSLTGRKEPLIVAHAEAASWYSCGPTVYDHAHLGHACSYVRFDIIRRILTKVfGCNIVMVMGITDVDDKIIKRANEM 131
Cdd:COG0215 3 KLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYL-GYKVTYVRNITDVDDKIIKRAAEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 132 NISPASLASLYEEDFKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGHAYsTAKGNVYFDLKSRGDkYGKLVGVVP 211
Cdd:COG0215 82 GESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAY-EADGDVYFDVRSFPD-YGKLSGRNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 212 -----GPVGEPaDSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQLDIHSGGIDLAFPHHENEI 286
Cdd:COG0215 160 ddlraGARVEV-DEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 287 AQCEVFHqCEQWGNYFLHSGHLHVKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAIDYSDSAMLHAQQQL 366
Cdd:COG0215 239 AQSEAAT-GKPFARYWMHNGFLTVNG--EKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKAL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 367 LALGSFLEDARAYMKGQLACGsvrevmlwERLASTRSAVKEALADDFDTPRVVDAILGLAHHGNGQLRAASkepgvprSP 446
Cdd:COG0215 316 ERLYNALRRLEEALGAADSSA--------EEIEELREEFIAAMDDDFNTPEALAVLFELVREINKALDEGE-------DK 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 447 AVFGAIISYFEQFFETVGISLGNQQCVSGDGSEATLRGVVEELVRFRQKVRQ---FALAkaeatgearrqqllerqplle 523
Cdd:COG0215 381 AALAALAALLRALGGVLGLLLLEPEAWQGAAEDELLDALIEALIEERAEARKakdFARA--------------------- 439
|
490 500
....*....|....*....|....*...
gi 1622884557 524 acDTLRQDLTAHGISIKDRNSTTsTWEL 551
Cdd:COG0215 440 --DRIRDELAALGIVLEDTPDGT-TWRR 464
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
53-550 |
6.21e-140 |
|
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not from all species. The enzyme from one archaeal species, Archaeoglobus fulgidus, is found but the equivalent enzymes from some other Archaea, including Methanococcus jannaschii, are not found, although biochemical evidence suggests that tRNA(Cys) in these species are charged directly with Cys rather than through a misacylation and correction pathway as for tRNA(Gln). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273076 [Multi-domain] Cd Length: 464 Bit Score: 413.32 E-value: 6.21e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 53 VYNSLTGRKEPLIVAHAEAASWYSCGPTVYDHAHLGHACSYVRFDIIRRILtKVFGCNIVMVMGITDVDDKIIKRANEMN 132
Cdd:TIGR00435 3 LYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYL-RYLGYKVQYVQNITDIDDKIIKRARENG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 133 ISPASLASLYEEDFKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGHAYSTAKGNVYFDLkSRGDKYGKLVG---- 208
Cdd:TIGR00435 82 ESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGDVYFDV-SKFKDYGKLSKqdld 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 209 -VVPGPVGEPaDSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQLDIHSGGIDLAFPHHENEIA 287
Cdd:TIGR00435 161 qLEAGARVDV-DEAKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 288 QCEVFHQcEQWGNYFLHSGHLHVKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAIDYSDSAMLHAQQQL- 366
Cdd:TIGR00435 240 QSEAAFG-KQLAKYWMHNGFLMIDN--EKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEAAKNALe 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 367 ---LALGSFLEDArAYMKGQLACGSVREVMLwerlastRSAVKEALADDFDTPRVVDAILGLAHHGNGQlraaskepgvP 443
Cdd:TIGR00435 317 rlyKALRVLDTSL-AYSGNQSLNKFPDEKEF-------EARFVEAMDDDLNTANALAVLFELAKSINLT----------F 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 444 RSPAVFGAIISYFEQFFETVGISLGNQQcvsgdgseatlrgvveelvRFRQKVRQFALAKAEATGEARRQQLLERQplLE 523
Cdd:TIGR00435 379 VSKADAALLIEHLIFLESRLGLLLGLPS-------------------KPVQAGSNDDLGEIEALIEERSIARKEKD--FA 437
|
490 500
....*....|....*....|....*..
gi 1622884557 524 ACDTLRQDLTAHGISIKDRNSTTsTWE 550
Cdd:TIGR00435 438 KADEIRDELAKKGIVLEDTPQGT-TWR 463
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
63-363 |
9.42e-137 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 399.05 E-value: 9.42e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 63 PLIVAHAEAASWYSCGPTVYDHAHLGHACSYVRFDIIRRILtKVFGCNIVMVMGITDVDDKIIKRANEMNISPASLASLY 142
Cdd:pfam01406 1 FFVPLHQGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYL-QALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 143 EEDFKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGHAYSTAKGNVYFDlKSRGDKYGKLVGVVPGPV----GEPA 218
Cdd:pfam01406 80 IEAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNGDVYFD-VSSFPDYGKLSGQNLEQLeagaRGEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 219 DSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQLDIHSGGIDLAFPHHENEIAQCEVFHQcEQW 298
Cdd:pfam01406 159 SEGKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFD-KQL 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622884557 299 GNYFLHSGHLHVKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAIDYSDSAMLHAQ 363
Cdd:pfam01406 238 ANYWLHNGHVMIDG--EKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSEELLEQAK 300
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
52-355 |
3.10e-114 |
|
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173899 [Multi-domain] Cd Length: 213 Bit Score: 338.01 E-value: 3.10e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 52 QVYNSLTGRKEPLIVAHAEAASWYSCGPTVYDHAHLGHACSYVRFDIIRRILTKvFGCNIVMVMGITDVDDKIIKRANEM 131
Cdd:cd00672 1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLED-LGYKVRYVQNITDIDDKIIKRAREE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 132 NISPASLASLYEEDFKQDMAALKVLPPAVYLRVtenipqiisfiegiiarghaystakgnvyfdlksrgdkygklvgvvp 211
Cdd:cd00672 80 GLSWKEVADYYTKEFFEDMKALNVLPPDVVPRV----------------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 212 gpvgepadsdkrhasdfalwkaakpqevfwaspwgpgrpgWHIECSAIASMVFGSQLDIHSGGIDLAFPHHENEIAQCEV 291
Cdd:cd00672 113 ----------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQSEA 152
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622884557 292 FHQcEQWGNYFLHSGHLHVKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAIDYS 355
Cdd:cd00672 153 ATG-KPFARYWLHTGHLTIDG--EKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
44-549 |
1.01e-97 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 308.01 E-value: 1.01e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 44 PTGRETGVQVYNSLTGRKEPLIVAHAEAASWYSCGPTVYDHAHLGHACSYVRFDIIRRILtKVFGCNIVMVMGITDVDDK 123
Cdd:PLN02946 53 PASRGRELHLYNTMSRKKELFKPKVEGKVGMYVCGVTAYDLSHIGHARVYVTFDVLYRYL-KHLGYEVRYVRNFTDVDDK 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 124 IIKRANEMNISPASLASLYEEDFKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGHAYSTaKGNVYFDLKsRGDKY 203
Cdd:PLN02946 132 IIARANELGEDPISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRV-DGDVYFSVD-KFPEY 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 204 GKLVG--VVPGPVGE--PADSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQLDIHSGGIDLAF 279
Cdd:PLN02946 210 GKLSGrkLEDNRAGErvAVDSRKKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDLVF 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 280 PHHENEIAQ----CevfhqCEQWGNYFLHSGHLHVkgKEEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAIDYS 355
Cdd:PLN02946 290 PHHENEIAQscaaC-----CDSNISYWIHNGFVTV--DSEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYS 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 356 DSAMLHAQQQLLALGSFLEDARAYMKGQ---LACGSVREVMLwERLASTRSAVKEALADDFDTPRVVDAILGLAHHGNGQ 432
Cdd:PLN02946 363 DVQLESASERIFYIYQTLHDCEESLQQHdstFEKDSVPPDTL-NCINKFHDEFVTSMSDDLHTPVALAALSEPLKTINDL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 433 LRAASKEPGVPRSPAvfgaiISYFEQFFETVGISLGnqqCVSGDGSEATlrgvveelvrfrQKVRQFALAKAEATGEARR 512
Cdd:PLN02946 442 LHTRKGKKQEKRLES-----LAALEKKIRDVLSVLG---LMPTSYSEAL------------QQLREKALRRAKLTEEQVL 501
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1622884557 513 QQLLERQPL-----LEACDTLRQDLTAHGISIKDRNSTTsTW 549
Cdd:PLN02946 502 QKIEERTVArknkeYEKSDAIRKDLAAVGIALMDSPDGT-TW 542
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
53-430 |
1.06e-84 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 277.75 E-value: 1.06e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 53 VYNSLTGRKEPLIVAHAEAASWYSCGPTVYDHAHLGHACSYVRFDIIRRILTKVfGCNIVMVMGITDVDDKIIKRANEMN 132
Cdd:PRK14535 230 IYNTLTRQKEPFAPIDPENVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLREC-GYPLTYVRNITDIDDKIIARAAENG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 133 ISPASLASLYEEDFKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGHAYSTAKGNVYFDLKSRGdKYGKLVGVVPG 212
Cdd:PRK14535 309 ETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYPAANGDVYYAVREFA-AYGQLSGKSLD 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 213 PV--GEPADSD--KRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQLDIHSGGIDLAFPHHENEIAQ 288
Cdd:PRK14535 388 DLraGERVEVDgfKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIAQ 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 289 --------CEVFHQCEQWGN-------YFLHSGHLHVKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAID 353
Cdd:PRK14535 468 svgatghtCGHHHAQTHHGQsiashvkYWLHNGFIRVDG--EKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLN 545
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622884557 354 YSDSAMLHAQQQLLALGSFLEDARAymkgqlacgsvREVMLWERLASTRSAVKEALADDFDTPRVVDAILGLAHHGN 430
Cdd:PRK14535 546 YSDAHLDDAKGALTRLYTTLKNTPA-----------AEFMLSENVNDYTRRFYAAMNDDFGTVEAVAVLFELAGEVN 611
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
51-550 |
4.00e-78 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 254.85 E-value: 4.00e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 51 VQVYNSLTGRKEPLIVAHAEAASWYSCGPTVYDHAHLGHACSYVRFDIIRRILtKVFGCNIVMVMGITDV---------- 120
Cdd:PRK14536 3 LRLYNTLGRQQEEFQPIEHGHVRLYGCGPTVYNYAHIGNLRTYVFQDTLRRTL-HFLGYRVTHVMNITDVghltddadsg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 121 DDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGHAYsTAKGNVYFDLKSRG 200
Cdd:PRK14536 82 EDKMVKSAQEHGKSVLEIAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTY-CAGGNVYFDIRTFP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 201 DkYGKLVGVVPGPVGEPA----DSDKRHASDFALW---KAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQLDIHSG 273
Cdd:PRK14536 161 S-YGSLASAAVEDLQAGAriehDTNKRNPHDFVLWftrSKFENHALTWDSPWGRGYPGWHIECSAMSMKYLGEQCDIHIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 274 GIDLAFPHHENEIAQCEVFhQCEQWGNYFLHSGHLHVkgKEEKMSKSLKNYITIKDFL-KTFSPDVFRFFCLRSSYRSAI 352
Cdd:PRK14536 240 GVDHIRVHHTNEIAQCEAA-TGKPWVRYWLHHEFLLM--NKGKMSKSAGQFLTLSSLQeKGFQPLDYRFFLLGGHYRSQL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 353 DYSDSAMLHAQQQLLALGSFLedARAYMKGQLACGSVREVM---LWERLASTRSAVKE--------ALADDFDTPRVVDA 421
Cdd:PRK14536 317 AFSWEALKTAKAARRSLVRRV--ARVVDAARATTGSVRGTLaecAAERVAESRASESEllltdfraALEDDFSTPKALSE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 422 ILGLAhhgngqlraasKEPGVPRspavfGAIISYFEQFFETVGISL--GNQQCVSGDGSEATLRGVVEELVRFRQKVRQ- 498
Cdd:PRK14536 395 LQKLV-----------KDTSVPP-----SLCLSVLQAMDTVLGLGLiqEATASLSAQVPAGPSEEEIGQLIEARAHARQt 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1622884557 499 --FALAkaeatgearrqqllerqplleacDTLRQDLTAHGISIKDRNSTTsTWE 550
Cdd:PRK14536 459 kdFPLA-----------------------DEIRDKLKAEGIELEDTHLGT-IWK 488
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
39-444 |
6.02e-71 |
|
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this protein family are MshC, l-cysteine:1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase, an enzyme that uses ATP to ligate a Cys residue to a mycothiol precursor molecule, in the second to last step in mycothiol biosynthesis. This enzyme shows considerable homology to Cys--tRNA ligases, and many instances are misannotated as such. Mycothiol is found in Mycobacterium tuberculosis, Corynebacterium glutamicum, Streptomyces coelicolor, and various other members of the Actinobacteria. Mycothiol is an analog to glutathione. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
Pssm-ID: 132488 [Multi-domain] Cd Length: 411 Bit Score: 233.46 E-value: 6.02e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 39 RAWLQPT-----GRETGVQVYNSLTGRKEPliVAHAEAASWYSCGPTVYDHAHLGHACSYVRFDIIRRILTKVfGCNIVM 113
Cdd:TIGR03447 1 QSWPAPAvpalpGTGPPLRLFDTADGQVRP--VEPGPEAGMYVCGITPYDATHLGHAATYLTFDLVNRVWRDA-GHRVHY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 114 VMGITDVDDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGHAY---STAKG 190
Cdd:TIGR03447 78 VQNVTDVDDPLFERAERDGVDWRELGTSQIDLFREDMEALRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYiveGPEYP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 191 NVYFDLKSrGDKYGKLVGVVPGPV--------GEPADSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASM 262
Cdd:TIGR03447 158 DVYFSIDA-TEQFGYESGYDRATMlelfaergGDPDRPGKRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 263 VFGSQLDIHSGGIDLAFPHHENEIAQCEVFHQCEQWGNYFLHSGHLHVKGkeEKMSKSLKNYITIKDFLKT-FSPDVFRF 341
Cdd:TIGR03447 237 RLGAGFDIQGGGSDLIFPHHEFSAAHAEAATGVRRMARHYVHAGMIGLDG--EKMSKSLGNLVFVSKLRAAgVDPAAIRL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 342 FCLRSSYRSAIDYSDSAMLHAQQQLlalgsfledarAYMKGQLACGSVREVmlwerlASTRSAVKEALADDFDTPRVVDA 421
Cdd:TIGR03447 315 GLLAGHYRQDRDWTDAVLAEAEARL-----------ARWRAALALPDAPDA------TDLIARLRQHLANDLDTPAALAA 377
|
410 420
....*....|....*....|...
gi 1622884557 422 ILGLAhhgNGQLRAASKEPGVPR 444
Cdd:TIGR03447 378 VDGWA---ADALSYGGSDTEAPA 397
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
66-422 |
3.68e-67 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 222.50 E-value: 3.68e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 66 VAHAEAASWYSCGPTVYDHAHLGHACSYVRFDIIRRILTKVfGCNIVMVMGITDVDDKIIKRANEMNISPASLASLYEED 145
Cdd:PRK12418 4 VAPGGTATMYVCGITPYDATHLGHAATYLAFDLVNRVWRDA-GHDVHYVQNVTDVDDPLLERAARDGVDWRDLAEREIAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 146 FKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGHAY---STAKGNVYFDLKSRGDkYGKLVGVVPGPV-------- 214
Cdd:PRK12418 83 FREDMEALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYvvdDEEYPDVYFSVDATPQ-FGYESGYDRATMlelfaerg 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 215 GEPADSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQLDIHSGGIDLAFPHHENEIAQCEVFHQ 294
Cdd:PRK12418 162 GDPDRPGKRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPHHEFSAAHAEAATG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 295 CEQWGNYFLHSGHLHVKGkeEKMSKSLKNYITIKDFLKT-FSPDVFRFFCLRSSYRSAIDYSDSAMLHAQQQL------L 367
Cdd:PRK12418 242 ERRFARHYVHAGMIGLDG--EKMSKSRGNLVFVSRLRAAgVDPAAIRLALLAGHYRADREWTDAVLAEAEARLarwraaA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1622884557 368 ALGSfLEDARAymkgqlacgsvrevmlwerlasTRSAVKEALADDFDTPRVVDAI 422
Cdd:PRK12418 320 ALPA-GPDAAD----------------------VVARVRAALADDLDTPGALAAV 351
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
75-355 |
1.23e-55 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 194.68 E-value: 1.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 75 YSCGPTVYDHAHLGHACSYVRFDIIRRILtKVFGCNIVMVMGITDV----------DDKIIKRANEMNISPASLASLYEE 144
Cdd:PRK14534 25 YACGPTVYNYAHIGNFRTYIFEDLLIKSL-RLLKYNVNYAMNITDIghltgdfddgEDKVVKAARERGLTVYEISRFFTE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 145 DFKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGHAYsTAKGNVYFDLkSRGDKYGKLVGVVPGPVGEPA------ 218
Cdd:PRK14534 104 AFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTY-FVNGNVYFDT-SCFKSYGQMAGINLNDFKDMSvsrvei 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 219 DSDKRHASDFALW---KAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQLDIHSGGIDLAFPHHENEIAQCEVFHQc 295
Cdd:PRK14534 182 DKSKRNKSDFVLWftnSKFKDQEMKWDSPWGFGYPSWHLECAAMNLEYFKSTLDIHLGGVDHIGVHHINEIAIAECYLN- 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622884557 296 EQWGNYFLHSGHLHVkgKEEKMSKSLKNYITIKDF-LKTFSPDVFRFFCLRSSYRSAIDYS 355
Cdd:PRK14534 261 KKWCDMFVHGEFLIM--EYEKMSKSNNNFITIKDLeDQGFSPLDFRYFCLTAHYRTQLKFT 319
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
305-430 |
3.54e-09 |
|
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439913 [Multi-domain] Cd Length: 544 Bit Score: 59.36 E-value: 3.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 305 SGHLHVKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLR-SSYRSAIDYSDSAMLHAQQQLLA--LGSFLEdaRA--- 378
Cdd:COG0143 318 HGFLTVEG--EKMSKSRGNVIDPDDLLDRYGPDALRYYLLReVPFGQDGDFSWEDFVARVNSDLAndLGNLAS--RTlsm 393
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622884557 379 ---YMKGQLACGSVREVM---LWERLASTRSAVKEALaDDFDTPRVVDAILGLAHHGN 430
Cdd:COG0143 394 ihkYFDGKVPEPGELTEAdeeLLAEAEAALEEVAEAM-EAFEFRKALEEIMALARAAN 450
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
305-347 |
2.24e-07 |
|
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) catalytic core domain. This class I enzyme aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. MetRS, which consists of the core domain and an anti-codon binding domain, functions as a monomer. However, in some species the anti-codon binding domain is followed by an EMAP domain. In this case, MetRS functions as a homodimer. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. As a result of a deletion event, MetRS has a significantly shorter core domain insertion than IleRS, ValRS, and LeuR. Consequently, the MetRS insertion lacks the editing function.
Pssm-ID: 173907 [Multi-domain] Cd Length: 319 Bit Score: 52.92 E-value: 2.24e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1622884557 305 SGHLHVKGKeeKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSS 347
Cdd:cd00814 271 HGYLTVEGK--KMSKSRGNVVDPDDLLERYGADALRYYLLRER 311
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
268-347 |
8.97e-07 |
|
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173906 [Multi-domain] Cd Length: 314 Bit Score: 51.09 E-value: 8.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 268 LDIHSGGIDLA--------FPHHeneiaqceVFHQCEQWGNY----FLHSGHLHVKGkeEKMSKSLKNYITIKDFLKTFS 335
Cdd:cd00812 225 VDIYIGGKEHApnhllysrFNHK--------ALFDEGLVTDEppkgLIVQGMVLLEG--EKMSKSKGNVVTPDEAIKKYG 294
|
90
....*....|..
gi 1622884557 336 PDVFRFFCLRSS 347
Cdd:cd00812 295 ADAARLYILFAA 306
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
305-357 |
8.50e-06 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 48.06 E-value: 8.50e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1622884557 305 SGHLHVKGKeeKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSA-IDYSDS 357
Cdd:pfam09334 315 HGYLTYEGG--KMSKSRGNVVWPSEALDRFPPDALRYYLARNRPETKdTDFSWE 366
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
315-366 |
5.46e-05 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 46.01 E-value: 5.46e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1622884557 315 EKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSS-YRSAIDYSDSAMLHAQQQL 366
Cdd:PRK12300 576 KKMSKSKGNVIPLRKAIEEYGADVVRLYLTSSAeLLQDADWREKEVESVRRQL 628
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
305-440 |
5.72e-05 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 45.91 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 305 SGHLHVKGkeEKMSKSlKNY-ITIKDFLKTFSPDVFRFFCL--RSSYRSAIDYSdsamLHAQQQ-----LLA-LGSFLed 375
Cdd:PRK00133 320 HGFLTVEG--AKMSKS-RGTfIWARTYLDHLDPDYLRYYLAakLPETIDDLDFN----WEDFQQrvnseLVGkVVNFA-- 390
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622884557 376 ARA------YMKGQLACGSVREVmLWERLASTRSAVKEALaDDFDTPRVVDAILGLAHHGNGQLraASKEP 440
Cdd:PRK00133 391 SRTagfinkRFDGKLPDALADPE-LLEEFEAAAEKIAEAY-EAREFRKALREIMALADFANKYV--DDNEP 457
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
75-149 |
7.08e-05 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 43.24 E-value: 7.08e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622884557 75 YSCGPTVYDHAHLGHACSYVRFDIIRRILTKVfGCNIVMVMGITDVDDKIIKRANEMNISPASLASLYEEDFKQD 149
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAYRKL-GYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKED 75
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
301-345 |
2.16e-04 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 44.10 E-value: 2.16e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1622884557 301 YFLHsGHLHVKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLR 345
Cdd:PRK11893 287 VFAH-GFLTLDG--EKMSKSLGNVIDPFDLVDEYGVDAVRYFLLR 328
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
311-422 |
2.24e-04 |
|
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439830 [Multi-domain] Cd Length: 931 Bit Score: 44.30 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 311 KGKeeKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAIDYSDSAMlhaQQQ-------------LLA-LGSFleDA 376
Cdd:COG0060 600 DGR--KMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSDEIL---KEVrdvyrrlrntyrfLLAnLDDF--DP 672
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1622884557 377 RAYMkgqLACGSVREVMLW--ERLASTRSAVKEALaDDFDTPRVVDAI 422
Cdd:COG0060 673 AEDA---VPYEDLPELDRWilSRLNELIKEVTEAY-DNYDFHRAYRAL 716
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
79-155 |
2.50e-04 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 43.72 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884557 79 PTVYDHAHLGHACSYVRFDIIRRILtKVFGCNivmVMGITDVDD---KIIKRANEMNISPASLASLYEEDFKQDMAALKV 155
Cdd:PRK11893 10 YYPNGKPHIGHAYTTLAADVLARFK-RLRGYD---VFFLTGTDEhgqKIQRKAEEAGISPQELADRNSAAFKRLWEALNI 85
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
296-343 |
5.07e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 43.13 E-value: 5.07e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1622884557 296 EQWGNYFLHSGHLHVKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFC 343
Cdd:PLN02959 700 EHWPRGFRCNGHLMLNS--EKMSKSTGNFLTLRQAIEEFSADATRFAL 745
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
312-355 |
1.56e-03 |
|
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too dissimilar to be included.
Pssm-ID: 459685 [Multi-domain] Cd Length: 602 Bit Score: 41.24 E-value: 1.56e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1622884557 312 GKEEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAIDYS 355
Cdd:pfam00133 559 EQGRKMSKSLGNVIDPLDVIDKYGADALRLWLANSDYGRDINLS 602
|
|
| LysS |
COG1384 |
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
315-355 |
2.99e-03 |
|
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA synthetase, class I is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440994 [Multi-domain] Cd Length: 525 Bit Score: 40.18 E-value: 2.99e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1622884557 315 EKMSKSLKNYITIKDFLKTFSPDVFRFFCLRsSYRSAIDYS 355
Cdd:COG1384 286 EKISKSKGNGLTVEEWLEYAEPESLRYFMFR-KPKKAKDLD 325
|
|
| tRNA-synt_1f |
pfam01921 |
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from ... |
309-353 |
3.81e-03 |
|
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from prokaryotes.
Pssm-ID: 396483 Cd Length: 357 Bit Score: 39.55 E-value: 3.81e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1622884557 309 HVKGKEeKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAID 353
Cdd:pfam01921 273 LLKGGG-KMSSSKGNVITPEDWLEYAPPESLRFLMFRTKPKKAKD 316
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
251-321 |
7.01e-03 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 37.07 E-value: 7.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622884557 251 GWHIECSAIASMVFGSQLDIHSGGIDLAFpHHENEIAQCEVFHQceQWGNYFLHSGHLHVKGKeEKMSKSL 321
Cdd:cd00802 77 EYMFLQAADFLLLYETECDIHLGGSDQLG-HIELGLELLKKAGG--PARPFGLTFGRVMGADG-TKMSKSK 143
|
|
| LysRS_core_class_I |
cd00674 |
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) ... |
309-346 |
8.60e-03 |
|
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. The class I LysRS is found only in archaea and some bacteria and has evolved separately from class II LysRS, as the two do not share structural or sequence similarity.
Pssm-ID: 173900 [Multi-domain] Cd Length: 353 Bit Score: 38.46 E-value: 8.60e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1622884557 309 HVKGKEeKMSKSLKNYITIKDFLKTFSPDVFRFFCLRS 346
Cdd:cd00674 269 GLKGGG-KMSSSKGNVITPSDWLEVAPPEVLRYLYARR 305
|
|
| |
